Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors

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From: Science(Vol. 259, Issue 5100)
Publisher: American Association for the Advancement of Science
Document Type: Article
Length: 2,950 words

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Abstract :

The actions of many hormones and neurotransmitters are mediated by the members of a superfamily of receptors coupled to heterotrimeric guanine nucleotide - binding proteins (G proteins). These receptors are characterized by a highly conserved topographical arrangement in which seven transmembrane domains are connected by intracellular and extracellular loops. The interaction between these receptors and G proteins is mediated in large part by the third intracellular loop of the receptor. Coexpression of the third intracellular loop of the [alpha.sub.1B]-adrenergic receptor with its parent receptor inhibited receptor-mediated activation of phospholipase C. The inhibition extended to the closely related [alpha.sub.c]-adrenergic receptor subtype, but not the phospholipase C - coupled M1 muscarinic acetylcholine receptor nor the adenylate cyclase - coupled [D.sub.1A] dopamine receptor. These results suggest that the receptor - G protein interface may represent a target for receptor antagonist drugs.

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Gale Document Number: GALE|A13620517